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Literature summary extracted from

  • Petrusma, M.; van der Geize, R.; Dijkhuizen, L.
    3-Ketosteroid 9alpha-hydroxylase enzymes Rieske non-heme monooxygenases essential for bacterial steroid degradation (2014), Antonie van Leeuwenhoek, 106, 157-172 .
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
1.14.15.30 drug development the enzyme can be a target for inhibition in treatment of tuberculosis Mycobacterium tuberculosis
1.14.15.30 medicine KSH inhibitory compounds may find application in combatting tuberculosis Mycobacterium tuberculosis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.15.30 gene kshA1, Rhodococcus jostii RHA1 encodes four sterol catabolic gene clusters, each of which contains a kshA gene, namely ro04538 (kshA1), ro02490 (kshA2), ro05811 (kshA3) and ro09003 (kshA4) Rhodococcus jostii
1.14.15.30 gene kshA2, Rhodococcus jostii RHA1 encodes four sterol catabolic gene clusters, each of which contains a kshA gene, namely ro04538 (kshA1), ro02490 (kshA2), ro05811 (kshA3) and ro09003 (kshA4) Rhodococcus jostii
1.14.15.30 gene kshA3, Rhodococcus jostii RHA1 encodes four sterol catabolic gene clusters, each of which contains a kshA gene, namely ro04538 (kshA1), ro02490 (kshA2), ro05811 (kshA3) and ro09003 (kshA4) Rhodococcus jostii
1.14.15.30 gene kshA4, Rhodococcus jostii RHA1 encodes four sterol catabolic gene clusters, each of which contains a kshA gene, namely ro04538 (kshA1), ro02490 (kshA2), ro05811 (kshA3) and ro09003 (kshA4) Rhodococcus jostii
1.14.15.30 Rhodococcus rhodochrous DSM43269 expresses 5 KshA homologues Rhodococcus rhodochrous

Protein Variants

EC Number Protein Variants Comment Organism
1.14.15.30 additional information a kshA null mutant is constructed by gene deletion mutagenesis (strain RG32) to fully block opening of the steroids polycyclic ring structure of cholesterol and beta-sitosterol resulting in accumulation of 1,4-androstadiene-3,17-dione and 3-oxo-23,24-bisnorchola-1,4-dien-22-oic acid Rhodococcus rhodochrous

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.15.30 Fe2+ contains non-heme Fe2+ Mycobacterium tuberculosis
1.14.15.30 Fe2+ the oxygenase component, which performs the substrate hydroxylation, is an iron-sulfur protein and contains a non-heme iron situated at the active site. The iron is bidentate bound to the carboxyl group of the aspartate leaving two sites available for exogenous ligands. This metal centre is more labile compared to the covalently bound heme-iron. Non-heme iron is a highly catalytic platform able to bind O2 and steroid substrate simultaneously in different orientations Mycolicibacterium smegmatis
1.14.15.30 Fe2+ the oxygenase component, which performs the substrate hydroxylation, is an iron-sulfur protein and contains a non-heme iron situated at the active site. The iron is bidentate bound to the carboxyl group of the aspartate leaving two sites available for exogenous ligands. This metal centre is more labile compared to the covalently bound heme-iron. Non-heme iron is a highly catalytic platform able to bind O2 and steroid substrate simultaneously in different orientations Rhodococcus rhodochrous
1.14.15.30 Fe2+ the oxygenase component, which performs the substrate hydroxylation, is an iron-sulfur protein and contains a non-heme iron situated at the active site. The iron is bidentate bound to the carboxyl group of the aspartate leaving two sites available for exogenous ligands. This metal centre is more labile compared to the covalently bound heme-iron. Non-heme iron is a highly catalytic platform able to bind O2 and steroid substrate simultaneously in different orientations Rhodococcus erythropolis
1.14.15.30 Fe2+ the oxygenase component, which performs the substrate hydroxylation, is an iron-sulfur protein and contains a non-heme iron situated at the active site. The iron is bidentate bound to the carboxyl group of the aspartate leaving two sites available for exogenous ligands. This metal centre is more labile compared to the covalently bound heme-iron. Non-heme iron is a highly catalytic platform able to bind O2 and steroid substrate simultaneously in different orientations Rhodococcus jostii
1.14.15.30 Fe2+ the oxygenase component, which performs the substrate hydroxylation, is an iron-sulfur protein and contains a non-heme iron situated at the active site. The iron is bidentate bound to the carboxyl group of the aspartate leaving two sites available for exogenous ligands. This metal centre is more labile compared to the covalently bound heme-iron. Non-heme iron is a highly catalytic platform able to bind O2 and steroid substrate simultaneously in different orientations Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.15.30 1,4-androstadiene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 Mycolicibacterium smegmatis
-
9alpha-hydroxy-1,4-androstadiene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
1.14.15.30 1,4-androstadiene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 Rhodococcus rhodochrous
-
9alpha-hydroxy-1,4-androstadiene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
1.14.15.30 1,4-androstadiene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 Rhodococcus erythropolis
-
9alpha-hydroxy-1,4-androstadiene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
1.14.15.30 1,4-androstadiene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 Rhodococcus jostii
-
9alpha-hydroxy-1,4-androstadiene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
1.14.15.30 1,4-androstadiene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 Mycobacterium tuberculosis
-
9alpha-hydroxy-1,4-androstadiene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
1.14.15.30 1,4-androstadiene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 Mycolicibacterium smegmatis mc2 155
-
9alpha-hydroxy-1,4-androstadiene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
1.14.15.30 1,4-androstadiene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 Rhodococcus erythropolis SQ1
-
9alpha-hydroxy-1,4-androstadiene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
1.14.15.30 1,4-androstadiene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 Mycobacterium tuberculosis H37Rv
-
9alpha-hydroxy-1,4-androstadiene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
1.14.15.30 1,4-androstadiene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 Rhodococcus rhodochrous DSM 43269
-
9alpha-hydroxy-1,4-androstadiene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
1.14.15.30 4-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 Mycolicibacterium smegmatis
-
9alpha-hydroxy-4-androstene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
1.14.15.30 4-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 Rhodococcus rhodochrous
-
9alpha-hydroxy-4-androstene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
1.14.15.30 4-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 Rhodococcus erythropolis
-
9alpha-hydroxy-4-androstene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
1.14.15.30 4-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 Rhodococcus jostii
-
9alpha-hydroxy-4-androstene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
1.14.15.30 4-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 Mycobacterium tuberculosis
-
9alpha-hydroxy-4-androstene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
1.14.15.30 4-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 Mycolicibacterium smegmatis mc2 155
-
9alpha-hydroxy-4-androstene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
1.14.15.30 4-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 Rhodococcus erythropolis SQ1
-
9alpha-hydroxy-4-androstene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
1.14.15.30 4-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 Mycobacterium tuberculosis H37Rv
-
9alpha-hydroxy-4-androstene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
1.14.15.30 4-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 Rhodococcus rhodochrous DSM 43269
-
9alpha-hydroxy-4-androstene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.14.15.30 Mycobacterium tuberculosis P71875
-
-
1.14.15.30 Mycobacterium tuberculosis P71875 isoform KshA
-
1.14.15.30 Mycobacterium tuberculosis H37Rv P71875
-
-
1.14.15.30 Mycobacterium tuberculosis H37Rv P71875 isoform KshA
-
1.14.15.30 Mycolicibacterium smegmatis
-
-
-
1.14.15.30 Mycolicibacterium smegmatis mc2 155
-
-
-
1.14.15.30 Rhodococcus erythropolis
-
-
-
1.14.15.30 Rhodococcus erythropolis SQ1
-
-
-
1.14.15.30 Rhodococcus jostii
-
-
-
1.14.15.30 Rhodococcus jostii Q0RXD9
-
-
1.14.15.30 Rhodococcus jostii Q0S812
-
-
1.14.15.30 Rhodococcus rhodochrous
-
-
-
1.14.15.30 Rhodococcus rhodochrous DSM 43269
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.14.15.30 androsta-1,4-diene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = 9alpha-hydroxyandrosta-1,4-diene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O KSH enzymes employ an electron transport chain that starts with the oxidation of NADH. The electrons are transferred to the flavin cofactor (FAD) of the ferredoxin reductase component KshB and then transported to the plant type iron-sulfur cluster of KshB. The Rieske iron-sulfur cluster of the KshA oxygenase component subsequently accepts the electrons from KshB. The electrons end up at the nonheme iron situated in the active site of KshA. The mononuclear iron is the site where O2 is bound and activated and the substrate is hydroxylated Rhodococcus rhodochrous
1.14.15.30 androsta-1,4-diene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = 9alpha-hydroxyandrosta-1,4-diene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O KSH enzymes employ an electron transport chain that starts with the oxidation of NADH. The electrons are transferred to the flavin cofactor (FAD) of the ferredoxin reductase component KshB and then transported to the plant type iron-sulfur cluster of KshB. The Rieske iron-sulfur cluster of the KshA oxygenase component subsequently accepts the electrons from KshB. The electrons end up at the nonheme iron situated in the active site of KshA. The mononuclear iron is the site where O2 is bound and activated and the substrate is hydroxylated Rhodococcus jostii
1.14.15.30 androsta-1,4-diene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = 9alpha-hydroxyandrosta-1,4-diene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O KSH enzymes employ an electron transport chain that starts with the oxidation of NADH. The electrons are transferred to the flavin cofactor (FAD) of the ferredoxin reductase component KshB and then transported to the plant type iron-sulfur cluster of KshB. The Rieske iron-sulfur cluster of the KshA oxygenase component subsequently accepts the electrons from KshB. The electrons end up at the nonheme iron situated in the active site of KshA. The mononuclear iron is the site where O2 is bound and activated and the substrate is hydroxylated Mycobacterium tuberculosis
1.14.15.30 androsta-1,4-diene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = 9alpha-hydroxyandrosta-1,4-diene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O KSH enzymes employ an electron transport chain that starts with the oxidation of NADH. The electrons are transferred to the flavin cofactor (FAD) of the ferredoxin reductase component KshB and then transported to the plant type iron-sulfur cluster of KshB. The Rieske ironĀ–sulfur cluster of the KshA oxygenase component subsequently accepts the electrons from KshB. The electrons end up at the nonheme iron situated in the active site of KshA. The mononuclear iron is the site where O2 is bound and activated and the substrate is hydroxylated Mycolicibacterium smegmatis
1.14.15.30 androsta-1,4-diene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = 9alpha-hydroxyandrosta-1,4-diene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O KSH enzymes employ an electron transport chain that starts with the oxidation of NADH. The electrons are transferred to the flavin cofactor (FAD) of the ferredoxin reductase component KshB and then transported to the plant type iron-sulfur cluster of KshB. The Rieske ironĀ–sulfur cluster of the KshA oxygenase component subsequently accepts the electrons from KshB. The electrons end up at the nonheme iron situated in the active site of KshA. The mononuclear iron is the site where O2 is bound and activated and the substrate is hydroxylated Rhodococcus erythropolis
1.14.15.30 androsta-1,4-diene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = 9alpha-hydroxyandrosta-1,4-diene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O KSH enzymes employ an electron transport chain that starts with the oxidation of NADH. The electrons are transferred to the flavin cofactor (FAD) of the ferredoxin reductase component KshB and then transported to the plant type iron-sulfur cluster of KshB. The Rieske ironĀ–sulfur cluster of the KshA oxygenase component subsequently accepts the electrons from KshB. The electrons end up at the nonheme iron situated in the active site of KshA. The mononuclear iron is the site where O2 is bound and activated and the substrate is hydroxylated Rhodococcus jostii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.15.30 1,4-androstadiene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
-
Mycolicibacterium smegmatis 9alpha-hydroxy-1,4-androstadiene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
1.14.15.30 1,4-androstadiene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
-
Rhodococcus rhodochrous 9alpha-hydroxy-1,4-androstadiene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
1.14.15.30 1,4-androstadiene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
-
Rhodococcus erythropolis 9alpha-hydroxy-1,4-androstadiene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
1.14.15.30 1,4-androstadiene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
-
Rhodococcus jostii 9alpha-hydroxy-1,4-androstadiene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
1.14.15.30 1,4-androstadiene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
-
Mycobacterium tuberculosis 9alpha-hydroxy-1,4-androstadiene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
1.14.15.30 1,4-androstadiene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
-
Mycolicibacterium smegmatis mc2 155 9alpha-hydroxy-1,4-androstadiene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
1.14.15.30 1,4-androstadiene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
-
Rhodococcus erythropolis SQ1 9alpha-hydroxy-1,4-androstadiene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
1.14.15.30 1,4-androstadiene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
-
Mycobacterium tuberculosis H37Rv 9alpha-hydroxy-1,4-androstadiene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
1.14.15.30 1,4-androstadiene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
-
Rhodococcus rhodochrous DSM 43269 9alpha-hydroxy-1,4-androstadiene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
1.14.15.30 1,4-androstadiene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + O2
-
Mycobacterium tuberculosis 9alpha-hydroxy-1,4-androstadiene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
1.14.15.30 1,4-androstadiene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + O2
-
Mycobacterium tuberculosis H37Rv 9alpha-hydroxy-1,4-androstadiene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
1.14.15.30 4-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
-
Mycolicibacterium smegmatis 9alpha-hydroxy-4-androstene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
1.14.15.30 4-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
-
Rhodococcus rhodochrous 9alpha-hydroxy-4-androstene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
1.14.15.30 4-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
-
Rhodococcus erythropolis 9alpha-hydroxy-4-androstene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
1.14.15.30 4-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
-
Rhodococcus jostii 9alpha-hydroxy-4-androstene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
1.14.15.30 4-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
-
Mycobacterium tuberculosis 9alpha-hydroxy-4-androstene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
1.14.15.30 4-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
-
Mycolicibacterium smegmatis mc2 155 9alpha-hydroxy-4-androstene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
1.14.15.30 4-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
-
Rhodococcus erythropolis SQ1 9alpha-hydroxy-4-androstene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
1.14.15.30 4-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
-
Mycobacterium tuberculosis H37Rv 9alpha-hydroxy-4-androstene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
1.14.15.30 4-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
-
Rhodococcus rhodochrous DSM 43269 9alpha-hydroxy-4-androstene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
1.14.15.30 additional information KSH of Mycobacterium tuberculosis can use 3-ketosteroids as substrates and shows high preference for the CoA thioester intermediate of cholesterol side chain degradation compared to the tested C17-ketosteroids Mycobacterium tuberculosis ?
-
?
1.14.15.30 additional information KSH of Rhodococcus rhodochrous can use 3-ketosteroids as substrates and shows high preference for the CoA thioester intermediate of cholesterol side chain degradation compared to the tested C17-ketosteroids Rhodococcus rhodochrous ?
-
?
1.14.15.30 additional information KSH of Mycobacterium tuberculosis can use 3-ketosteroids as substrates and shows high preference for the CoA thioester intermediate of cholesterol side chain degradation compared to the tested C17-ketosteroids Mycobacterium tuberculosis H37Rv ?
-
?
1.14.15.30 additional information KSH of Rhodococcus rhodochrous can use 3-ketosteroids as substrates and shows high preference for the CoA thioester intermediate of cholesterol side chain degradation compared to the tested C17-ketosteroids Rhodococcus rhodochrous DSM 43269 ?
-
?

Subunits

EC Number Subunits Comment Organism
1.14.15.30 More typical head-to-tail trimer arrangement of KshA enzymes, structure overview Mycolicibacterium smegmatis
1.14.15.30 More typical head-to-tail trimer arrangement of KshA enzymes, structure overview Rhodococcus rhodochrous
1.14.15.30 More typical head-to-tail trimer arrangement of KshA enzymes, structure overview Rhodococcus erythropolis
1.14.15.30 More typical head-to-tail trimer arrangement of KshA enzymes, structure overview Rhodococcus jostii
1.14.15.30 More typical head-to-tail trimer arrangement of KshA enzymes, structure overview Mycobacterium tuberculosis

Synonyms

EC Number Synonyms Comment Organism
1.14.15.30 3-ketosteroid 9-alpha-hydroxylase
-
Mycobacterium tuberculosis
1.14.15.30 3-ketosteroid 9alpha-hydroxylase
-
Mycolicibacterium smegmatis
1.14.15.30 3-ketosteroid 9alpha-hydroxylase
-
Rhodococcus rhodochrous
1.14.15.30 3-ketosteroid 9alpha-hydroxylase
-
Rhodococcus erythropolis
1.14.15.30 3-ketosteroid 9alpha-hydroxylase
-
Rhodococcus jostii
1.14.15.30 3-ketosteroid 9alpha-hydroxylase
-
Mycobacterium tuberculosis
1.14.15.30 KSH
-
Mycolicibacterium smegmatis
1.14.15.30 KSH
-
Rhodococcus rhodochrous
1.14.15.30 KSH
-
Rhodococcus erythropolis
1.14.15.30 KSH
-
Rhodococcus jostii
1.14.15.30 KSH
-
Mycobacterium tuberculosis
1.14.15.30 KshA
-
Mycobacterium tuberculosis
1.14.15.30 KshA
-
Rhodococcus jostii
1.14.15.30 KshA1
-
Rhodococcus jostii
1.14.15.30 KshA2
-
Rhodococcus jostii
1.14.15.30 KshA3
-
Rhodococcus jostii
1.14.15.30 KshA4
-
Rhodococcus jostii
1.14.15.30 KshB
-
Mycobacterium tuberculosis

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.15.30 FAD flavin co-factor of the ferredoxin reductase component KshB Mycolicibacterium smegmatis
1.14.15.30 FAD flavin co-factor of the ferredoxin reductase component KshB Rhodococcus rhodochrous
1.14.15.30 FAD flavin co-factor of the ferredoxin reductase component KshB Rhodococcus erythropolis
1.14.15.30 FAD flavin co-factor of the ferredoxin reductase component KshB Rhodococcus jostii
1.14.15.30 FAD flavin co-factor of the ferredoxin reductase component KshB Mycobacterium tuberculosis
1.14.15.30 [2Fe-2S]-center a Rieske iron-sulfur cluster of the KshA oxygenase component and a plant type iron-sulfur cluster of KshB. The oxygenase component, which performs the substrate hydroxylation, is an iron-sulfur protein and contains a non-heme iron situated at the active site. The Rieske iron-sulfur cluster and the non-heme Fe2+ catalytic centre are located relatively far away from each other, but the typical head-to-tail trimer arrangement positions the Rieske Fe2-S2 in close proximity to the non-heme Fe2+ of the neighbouring KshA subunit, enabling transport of electrons between KshA subunits Mycolicibacterium smegmatis
1.14.15.30 [2Fe-2S]-center a Rieske iron-sulfur cluster of the KshA oxygenase component and a plant type iron-sulfur cluster of KshB. The oxygenase component, which performs the substrate hydroxylation, is an iron-sulfur protein and contains a non-heme iron situated at the active site. The Rieske iron-sulfur cluster and the non-heme Fe2+ catalytic centre are located relatively far away from each other, but the typical head-to-tail trimer arrangement positions the Rieske Fe2-S2 in close proximity to the non-heme Fe2+ of the neighbouring KshA subunit, enabling transport of electrons between KshA subunits Rhodococcus rhodochrous
1.14.15.30 [2Fe-2S]-center a Rieske iron-sulfur cluster of the KshA oxygenase component and a plant type iron-sulfur cluster of KshB. The oxygenase component, which performs the substrate hydroxylation, is an iron-sulfur protein and contains a non-heme iron situated at the active site. The Rieske iron-sulfur cluster and the non-heme Fe2+ catalytic centre are located relatively far away from each other, but the typical head-to-tail trimer arrangement positions the Rieske Fe2-S2 in close proximity to the non-heme Fe2+ of the neighbouring KshA subunit, enabling transport of electrons between KshA subunits Rhodococcus erythropolis
1.14.15.30 [2Fe-2S]-center a Rieske iron-sulfur cluster of the KshA oxygenase component and a plant type iron-sulfur cluster of KshB. The oxygenase component, which performs the substrate hydroxylation, is an iron-sulfur protein and contains a non-heme iron situated at the active site. The Rieske iron-sulfur cluster and the non-heme Fe2+ catalytic centre are located relatively far away from each other, but the typical head-to-tail trimer arrangement positions the Rieske Fe2-S2 in close proximity to the non-heme Fe2+ of the neighbouring KshA subunit, enabling transport of electrons between KshA subunits Rhodococcus jostii
1.14.15.30 [2Fe-2S]-center a Rieske iron-sulfur cluster of the KshA oxygenase component and a plant type iron-sulfur cluster of KshB. The oxygenase component, which performs the substrate hydroxylation, is an iron-sulfur protein and contains a non-heme iron situated at the active site. The Rieske iron-sulfur cluster and the non-heme Fe2+ catalytic centre are located relatively far away from each other, but the typical head-to-tail trimer arrangement positions the Rieske Fe2-S2 in close proximity to the non-heme Fe2+ of the neighbouring KshA subunit, enabling transport of electrons between KshA subunits Mycobacterium tuberculosis
1.14.15.30 [2Fe-2S]-center a Rieske iron-sulfur cluster of the KshA oxygenase component and a plant type iron-sulfur cluster of KshB. The oxygenase component, which performs the substrate hydroxylation, is an ironsulfur protein and contains a non-heme iron situated at the active site. The Rieske iron-sulfur cluster and the non-heme Fe2+ catalytic centre are located relatively far away from each other, but the typical head-to-tail trimer arrangement positions the Rieske Fe2-S2 in close proximity to the non-heme Fe2+ of the neighbouring KshA subunit, enabling transport of electrons between KshA subunits Rhodococcus jostii

General Information

EC Number General Information Comment Organism
1.14.15.30 evolution KSH is classified as a group I RO in this classification system. Group I contains a broad range of mono- and dioxygenases with low amino acid sequence similarity and various protein sizes. The oxygenases are alpha-monomers. KshA contains a Rieske domain, coordinating the Rieske Fe2-S2 cluster, and a catalytic domain with the typical helix-Grip fold, which is part of the StAR (steroidogenic acute regulatory protein) related lipid transfer (START) domain superfamily. The catalytic domain is composed of a beta-sheet flanked by alpha-helices Mycolicibacterium smegmatis
1.14.15.30 evolution KSH is classified as a group I RO in this classification system. Group I contains a broad range of mono- and dioxygenases with low amino acid sequence similarity and various protein sizes. The oxygenases are alpha-monomers. KshA contains a Rieske domain, coordinating the Rieske Fe2-S2 cluster, and a catalytic domain with the typical helix-Grip fold, which is part of the StAR (steroidogenic acute regulatory protein) related lipid transfer (START) domain superfamily. The catalytic domain is composed of a beta-sheet flanked by alpha-helices Rhodococcus rhodochrous
1.14.15.30 evolution KSH is classified as a group I RO in this classification system. Group I contains a broad range of mono- and dioxygenases with low amino acid sequence similarity and various protein sizes. The oxygenases are alpha-monomers. KshA contains a Rieske domain, coordinating the Rieske Fe2-S2 cluster, and a catalytic domain with the typical helix-Grip fold, which is part of the StAR (steroidogenic acute regulatory protein) related lipid transfer (START) domain superfamily. The catalytic domain is composed of a beta-sheet flanked by alpha-helices Rhodococcus erythropolis
1.14.15.30 evolution KSH is classified as a group I RO in this classification system. Group I contains a broad range of mono- and dioxygenases with low amino acid sequence similarity and various protein sizes. The oxygenases are alpha-monomers. KshA contains a Rieske domain, coordinating the Rieske Fe2-S2 cluster, and a catalytic domain with the typical helix-Grip fold, which is part of the StAR (steroidogenic acute regulatory protein) related lipid transfer (START) domain superfamily. The catalytic domain is composed of a beta-sheet flanked by alpha-helices Rhodococcus jostii
1.14.15.30 evolution KSH is classified as a group I RO in this classification system. Group I contains a broad range of mono- and dioxygenases with low amino acid sequence similarity and various protein sizes. The oxygenases are alpha-monomers. KshA contains a Rieske domain, coordinating the Rieske Fe2-S2 cluster, and a catalytic domain with the typical helix-Grip fold, which is part of the StAR (steroidogenic acute regulatory protein) related lipid transfer (START) domain superfamily. The catalytic domain is composed of a beta-sheet flanked by alpha-helices Mycobacterium tuberculosis
1.14.15.30 malfunction deletion of KSH activity in sterol degrading bacteria results in blockage of steroid ring opening and is used to produce valuable C19-steroids such as 4-androstene-3,17-dione and 1,4-androstadiene-3,17-dione Rhodococcus rhodochrous
1.14.15.30 malfunction deletion of KSH activity in sterol degrading bacteria results in blockage of steroid ring opening and is used to produce valuable C19-steroids such as 4-androstene-3,17-dione and 1,4-androstadiene-3,17-dione Rhodococcus erythropolis
1.14.15.30 malfunction deletion of KSH activity in sterol degrading bacteria results in blockage of steroid ring opening and is used to produce valuable C19-steroids such as 4-androstene-3,17-dione and 1,4-androstadiene-3,17-dione Rhodococcus jostii
1.14.15.30 malfunction deletion of KSH activity in sterol degrading bacteria results in blockage of steroid ring opening and is used to produce valuable C19-steroids such as 4-androstene-3,17-dione and 1,4-androstadiene-3,17-dione Mycobacterium tuberculosis
1.14.15.30 malfunction deletion of KSH activity in sterol degrading bacteria results in blockage of steroid ring opening and is used to produce valuable C19-steroids such as 4-androstene-3,17-dione and 1,4-androstadiene-3,17-dione. A kshA disruption mutant of Mycobacterium smegmatis mc2 155 incubated with sitosterol accumulates 4-androstene-3,17-dione and 1,4-androstadiene-3,17-dione Mycolicibacterium smegmatis
1.14.15.30 additional information structure-function relationship of KSH enzymes and components, overview Mycolicibacterium smegmatis
1.14.15.30 additional information structure-function relationship of KSH enzymes and components, overview Rhodococcus rhodochrous
1.14.15.30 additional information structure-function relationship of KSH enzymes and components, overview Rhodococcus erythropolis
1.14.15.30 additional information structure-function relationship of KSH enzymes and components, overview Rhodococcus jostii
1.14.15.30 additional information structure-function relationship of KSH enzymes and components, overview Mycobacterium tuberculosis
1.14.15.30 physiological function a plant type iron-sulfur cluster of KshB. The 3-ketosteroid 9alpha-hydroxylase activity is a two component Rieske non-heme monooxygenase comprised of the oxygenase KshA and the reductase KshB, and is a key enzyme in bacterial steroid degradation, essential for the pathogenicity of Mycobacterium tuberculosis. KSH initiates opening of the steroid polycyclic ring structure Mycolicibacterium smegmatis
1.14.15.30 physiological function a plant type iron-sulfur cluster of KshB. The 3-ketosteroid 9alpha-hydroxylase activity is a two component Rieske non-heme monooxygenase comprised of the oxygenase KshA and the reductase KshB, and is a key enzyme in bacterial steroid degradation, essential for the pathogenicity of Mycobacterium tuberculosis. KSH initiates opening of the steroid polycyclic ring structure Rhodococcus jostii
1.14.15.30 physiological function a plant type iron-sulfur cluster of KshB. The 3-ketosteroid 9alpha-hydroxylase activity is a two component Rieske non-heme monooxygenase comprised of the oxygenase KshA and the reductase KshB, and is a key enzyme in bacterial steroid degradation, essential for the pathogenicity of Mycobacterium tuberculosis. KSH initiates opening of the steroid polycyclic ring structure Mycobacterium tuberculosis
1.14.15.30 physiological function a plant type iron-sulfur cluster of KshB. The 3-ketosteroid 9alpha-hydroxylase activity is a two component Rieske non-heme monooxygenase comprised of the oxygenase KshA and the reductase KshB, and is a key-enzyme in bacterial steroid degradation, essential for the pathogenicity of Mycobacterium tuberculosis. KSH initiates opening of the steroid polycyclic ring structure Rhodococcus jostii
1.14.15.30 physiological function the 3-ketosteroid 9alpha-hydroxylase activity is a two component Rieske non-heme monooxygenase comprised of the oxygenase KshA and the reductase KshB, and is a key enzyme in bacterial steroid degradation. KSH initiates opening of the steroid polycyclic ring structure Rhodococcus rhodochrous
1.14.15.30 physiological function the 3-ketosteroid 9alpha-hydroxylase activity is a two component Rieske non-heme monooxygenase comprised of the oxygenase KshA and the reductase KshB, and is a key-enzyme in bacterial steroid degradation. KSH initiates opening of the steroid polycyclic ring structure Rhodococcus erythropolis
1.14.15.30 physiological function the enzyme is essential for the pathogenicity of Mycobacterium tuberculosis Mycobacterium tuberculosis